Evidence map›Paper›PMID 31457088›Full record

ArticleScience advances2019

Dynamic tuning of FRET in a green fluorescent protein biosensor.

Pablo Trigo-Mourino, Thomas Thestrup, Oliver Griesbeck, Christian Griesinger, Stefan Becker

Abstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

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  14. Lanthanide Tagging of Oligonucleotides to Nucleobase for Paramagnetic NMR.Chembiochem : a European journal of chemical biology · 2020
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Pablo Trigo-MourinoDepartment for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-0822-882X
Thomas ThestrupMax Planck Institute of Neurobiology, Martinsried, Germany.
Oliver GriesbeckMax Planck Institute of Neurobiology, Martinsried, Germany.
Christian GriesingerDepartment for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-1266-4344
Stefan BeckerDepartment for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-2041-5740

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Förster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with

Indexed as

Biosensing TechniquesFluorescence Resonance Energy TransferGreen Fluorescent ProteinsMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryRecombinant ProteinsScattering, Small AngleX-Ray DiffractionGreen Fluorescent ProteinsRecombinant Proteins

Identifiers

PMID31457088
PMCPMC6685724

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.